2G17
The structure of N-acetyl-gamma-glutamyl-phosphate reductase from Salmonella typhimurium.
Experimental procedure
| Experimental method | SAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-08-24 |
| Detector | SBC-2 |
| Wavelength(s) | 0.97937 |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 165.001, 165.001, 105.778 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.630 - 2.300 |
| R-factor | 0.17084 |
| Rwork | 0.170 |
| R-free | 0.19344 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.471 |
| Data scaling software | HKL-2000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Number of reflections | 37632 | |
| Completeness [%] | 98.7 | 95.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | 2M (NH4)SO4, 0.1M Tris pH7.0, 0.2M LiSO4, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
